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Literature summary for 3.4.21.89 extracted from

  • Powers, M.E.; Smith, P.A.; Roberts, T.C.; Fowler, B.J.; King, C.C.; Trauger, S.A.; Siuzdak, G.; Romesberg, F.E.
    Type I signal peptidase and protein secretion in Staphylococcus epidermidis (2011), J. Bacteriol., 193, 340-348.
    View publication on PubMedView publication on EuropePMC
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Inhibitors

Inhibitors Comment Organism Structure
arylomycin A2
-
 Staphylococcus epidermidis
arylomycin C16
-
 Staphylococcus epidermidis

Organism

Organism UniProt Comment Textmining
Staphylococcus epidermidis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-lactam response sensor BlaR1 + H2O presence of extracellular domains of beta-lactam response sensor BlaR1 in the medium is dependent on SPase activity, suggesting that it is cleaved at noncanonical sites within the protein Staphylococcus epidermidis ?
-
 ?
lipoteichoic acid synthase + H2O presence of extracellular domains of lipoteichoic acid synthase in the medium is dependent on SPase activity, suggesting that it is cleaved at noncanonical sites within the protein Staphylococcus epidermidis ?
-
 ?
additional information identification of 11 proteins whose secretion from stationary-phase Staphylococcus epidermidis is dependent on SPase activity. 9 of these are predicted to be translated with canonical N-terminal signal peptides. The presence of extracellular domains of lipoteichoic acid synthase and the beta-lactam response sensor BlaR1 in the medium is dependent on SPase activity, suggesting that they are cleaved at noncanonical sites within the protein Staphylococcus epidermidis ?
-
 ?

Synonyms

Synonyms Comment Organism
SPase
-
 Staphylococcus epidermidis